{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,30]],"date-time":"2026-06-30T23:34:27Z","timestamp":1782862467008,"version":"3.54.5"},"reference-count":28,"publisher":"American Association for the Advancement of Science (AAAS)","issue":"4226","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Science"],"published-print":{"date-parts":[[1976,2,6]]},"abstract":"<jats:p>\n            The hydration rate of CO\n            <jats:sub>2<\/jats:sub>\n            catalyzed by human red cell carbonic anhydrase B is 92 percent reduced by the normal concentrations of chloride and bicarbonate in red cells. This reflects a general sensitivity of this reaction to halides and other anions, up to 87 times greater than the effect on red cell carbonic anhydrase C. The catalytic hydration of CO\n            <jats:sub>2<\/jats:sub>\n            is generally more (up to 24 times) sensitive to inhibition by anions and sulfonamides than the dehydration of HCO\n            <jats:sub>3<\/jats:sub>\n            -, probably reflecting different mechanisms. The sensitivity of enzyme B to anion inhibition also depends upon the substrate, being much greater for CO\n            <jats:sub>2<\/jats:sub>\n            than for certain esters. On the basis of the very low catalytic activity of B for CO\n            <jats:sub>2<\/jats:sub>\n            in the presence of physiological concentration of chloride, and the fact that carbonic anhydrase C is effective for CO\n            <jats:sub>2<\/jats:sub>\n            hydration (in the presence of chloride) at a rate 340 times greater than that of CO\n            <jats:sub>2<\/jats:sub>\n            output from tissues, it appears that the biological role of enzyme B is not that of a carbonic anhydrase.\n          <\/jats:p>","DOI":"10.1126\/science.813299","type":"journal-article","created":{"date-parts":[[2006,10,5]],"date-time":"2006-10-05T15:51:28Z","timestamp":1160063488000},"page":"469-472","source":"Crossref","is-referenced-by-count":95,"title":["Inhibition by Anions of Human Red Cell Carbonic Anhydrase B: Physiological and Biochemical Implications"],"prefix":"10.1126","volume":"191","author":[{"given":"Thomas H.","family":"Maren","sequence":"first","affiliation":[{"name":"Department of Pharmacology and Therapeutics, University of Florida College of Medicine, Gainesville 32610"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Catherine S.","family":"Rayburn","sequence":"additional","affiliation":[{"name":"Department of Pharmacology and Therapeutics, University of Florida College of Medicine, Gainesville 32610"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Norman E.","family":"Liddell","sequence":"additional","affiliation":[{"name":"Department of Pharmacology and Therapeutics, University of Florida College of Medicine, Gainesville 32610"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"221","reference":[{"key":"e_1_2_1_1_1","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1111\/j.1469-185X.1972.tb01079.x","volume":"47","year":"1972","unstructured":"CARTER, M.J., CARBONIC-ANHYDRASE - ISOENZYMES, PROPERTIES, DISTRIBUTION, AND FUNCTIONAL SIGNIFICANCE, BIOLOGICAL REVIEWS OF THE CAMBRIDGE PHILOSOPHICAL SOCIETY 47: 465 (1972).","journal-title":"BIOLOGICAL REVIEWS OF THE CAMBRIDGE PHILOSOPHICAL SOCIETY"},{"key":"e_1_2_1_2_1","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1113\/jphysiol.1972.sp009716","volume":"220","year":"1972","unstructured":"CARTER, M. J., JOURNAL OF PHYSIOLOGY-LONDON 220: 465 (1972).","journal-title":"JOURNAL OF PHYSIOLOGY-LONDON"},{"key":"e_1_2_1_3_1","doi-asserted-by":"crossref","first-page":"630","DOI":"10.1016\/0005-2744(70)90298-6","volume":"220","year":"1970","unstructured":"CHRISTIANSEN, E, BIOCHIMICA ET BIOPHYSICA ACTA (BBA) - ENZYMOLOGY 220: 630 (1970).","journal-title":"BIOCHIMICA ET BIOPHYSICA ACTA (BBA) - ENZYMOLOGY"},{"key":"e_1_2_1_4_1","first-page":"488","volume":"1","year":"1973","unstructured":"Coleman, J. 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